Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 63, Part 3 (March 2007)

structural genomics communications

 

The structure of Plasmodium vivax phosphatidylethanolamine-binding protein suggests a functional motif containing a left-handed helix

T. Arakaki, H. Neely, E. Boni, N. Mueller, F. S. Buckner, W. C. Van Voorhis, A. Lauricella, G. DeTitta, J. Luft, W. G. J. Hol and E. A. Merritt

Abstract: The structure of a putative Raf kinase inhibitor protein (RKIP) homolog from the eukaryotic parasite Plasmodium vivax has been studied to a resolution of 1.3 Å using multiple-wavelength anomalous diffraction at the Se K edge. This protozoan protein is topologically similar to previously studied members of the phosphatidylethanolamine-binding protein (PEBP) sequence family, but exhibits a distinctive left-handed -helical region at one side of the canonical phospholipid-binding site. Re-examination of previously determined PEBP structures suggests that the P. vivax protein and yeast carboxypeptidase Y inhibitor may represent a structurally distinct subfamily of the diverse PEBP-sequence family.

PDB reference: 2gzq

Keywords: phosphatidylethanolamine-binding protein; Plasmodium vivax.

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